| UniProt ID | LYS4_YEAST | |
|---|---|---|
| UniProt AC | P49367 | |
| Protein Name | Homoaconitase, mitochondrial | |
| Gene Name | LYS4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 693 | |
| Subcellular Localization | Mitochondrion . | |
| Protein Description | Catalyzes the reversible hydration of cis-homoaconitate to (2R,3S)-homoisocitrate, a step in the alpha-aminoadipate pathway for lysine biosynthesis.. | |
| Protein Sequence | MLRSTTFTRSFHSSRAWLKGQNLTEKIVQSYAVNLPEGKVVHSGDYVSIKPAHCMSHDNSWPVALKFMGLGATKIKNPSQIVTTLDHDIQNKSEKNLTKYKNIENFAKKHHIDHYPAGRGIGHQIMIEEGYAFPLNMTVASDSHSNTYGGLGSLGTPIVRTDAAAIWATGQTWWQIPPVAQVELKGQLPQGVSGKDIIVALCGLFNNDQVLNHAIEFTGDSLNALPIDHRLTIANMTTEWGALSGLFPVDKTLIDWYKNRLQKLGTNNHPRINPKTIRALEEKAKIPKADKDAHYAKKLIIDLATLTHYVSGPNSVKVSNTVQDLSQQDIKINKAYLVSCTNSRLSDLQSAADVVCPTGDLNKVNKVAPGVEFYVAAASSEIEADARKSGAWEKLLKAGCIPLPSGCGPCIGLGAGLLEPGEVGISATNRNFKGRMGSKDALAYLASPAVVAASAVLGKISSPAEVLSTSEIPFSGVKTEIIENPVVEEEVNAQTEAPKQSVEILEGFPREFSGELVLCDADNINTDGIYPGKYTYQDDVPKEKMAQVCMENYDAEFRTKVHPGDIVVSGFNFGTGSSREQAATALLAKGINLVVSGSFGNIFSRNSINNALLTLEIPALIKKLREKYQGAPKELTRRTGWFLKWDVADAKVVVTEGSLDGPVILEQKVGELGKNLQEIIVKGGLEGWVKSQL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 26 | Ubiquitination | KGQNLTEKIVQSYAV HCCCHHHHHHHHHCC | 42.83 | 15699485 | |
| 39 | Ubiquitination | AVNLPEGKVVHSGDY CCCCCCCCEEECCCE | 39.15 | 15699485 | |
| 76 | Acetylation | GLGATKIKNPSQIVT CCCCCCCCCHHHHEE | 65.45 | 22865919 | |
| 92 | Acetylation | LDHDIQNKSEKNLTK ECHHHCCCCCCCCHH | 43.55 | 24489116 | |
| 95 | Acetylation | DIQNKSEKNLTKYKN HHCCCCCCCCHHHHC | 65.43 | 25381059 | |
| 101 | Acetylation | EKNLTKYKNIENFAK CCCCHHHHCHHHHHH | 53.67 | 25381059 | |
| 108 | Acetylation | KNIENFAKKHHIDHY HCHHHHHHHHCCCCC | 48.80 | 25381059 | |
| 258 | Acetylation | KTLIDWYKNRLQKLG HHHHHHHHHHHHHHC | 31.19 | 24489116 | |
| 321 | Phosphorylation | NSVKVSNTVQDLSQQ CCCCEECCCHHHHHC | 16.43 | 28889911 | |
| 340 | Glutathionylation | NKAYLVSCTNSRLSD CEEEEEECCCCCHHH | 3.05 | 22833525 | |
| 356 | Glutathionylation | QSAADVVCPTGDLNK HHHCCEECCCCCHHH | 2.22 | 22833525 | |
| 363 | Ubiquitination | CPTGDLNKVNKVAPG CCCCCHHHHCCCCCC | 55.25 | 15699485 | |
| 439 | Acetylation | FKGRMGSKDALAYLA CCCCCCCHHHHHHHH | 41.09 | 24489116 | |
| 542 | Acetylation | TYQDDVPKEKMAQVC CCCCCCCHHHHHHHH | 70.57 | 25381059 | |
| 622 | Acetylation | LEIPALIKKLREKYQ HHHHHHHHHHHHHHC | 46.75 | 24489116 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of LYS4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LYS4_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of LYS4_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| IF5A1_YEAST | HYP2 | physical | 16554755 | |
| ZUO1_YEAST | ZUO1 | physical | 16554755 | |
| SSZ1_YEAST | SSZ1 | physical | 16554755 | |
| HS104_YEAST | HSP104 | physical | 16554755 | |
| GLYC_YEAST | SHM2 | physical | 16554755 | |
| EF3A_YEAST | YEF3 | physical | 16554755 | |
| EF1G1_YEAST | CAM1 | physical | 16554755 | |
| KYNU_YEAST | BNA5 | genetic | 16941010 | |
| KMO_YEAST | BNA4 | genetic | 16941010 | |
| I23O_YEAST | BNA2 | genetic | 16941010 | |
| SDH3_YEAST | SDH3 | genetic | 16941010 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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